2pou: Difference between revisions

Revision as of 15:25, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2pou.png

Template:STRUCTURE 2pou

The crystal structure of the human carbonic anhydrase II in complex with 4,5-dichloro-benzene-1,3-disulfonamideThe crystal structure of the human carbonic anhydrase II in complex with 4,5-dichloro-benzene-1,3-disulfonamide

Template:ABSTRACT PUBMED 17540563

About this StructureAbout this Structure

2POU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides--solution and crystallographic studies., Alterio V, De Simone G, Monti SM, Scozzafava A, Supuran CT, Bioorg Med Chem Lett. 2007 Aug 1;17(15):4201-7. Epub 2007 May 18. PMID:17540563

Page seeded by OCA on Mon Jul 28 15:25:43 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2pou.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2pou|  PDB=2pou  |  SCENE=  }}
-'''The crystal structure of the human carbonic anhydrase II in complex with 4,5-dichloro-benzene-1,3-disulfonamide'''
+===The crystal structure of the human carbonic anhydrase II in complex with 4,5-dichloro-benzene-1,3-disulfonamide===
-==Overview==
+<!--
-Three benzene-1,3-disulfonamide derivatives were investigated for their interaction with 12 mammalian alpha-carbonic anhydrases (CAs, EC 4.2.1.1), and three bacterial/archaeal CAs belonging to the alpha-, beta-, and gamma-CA class, respectively. X-ray crystal structure of the three inhibitors in complex with the dominant human isozyme CA II revealed a particular binding mode within the cavity. The sulfonamide group in meta-position to the Zn(2+)-coordinated SO(2)NH(2) moiety was oriented toward the hydrophilic side of the active site cleft, establishing hydrogen bonds with His64, Asn67, Gln92, and Thr200. The plane of the phenyl moiety of the inhibitors was rotated by 45 degrees and tilted by 10 degrees with respect to its most recurrent orientation in other CA II-sulfonamide complexes.
+The line below this paragraph, {{ABSTRACT_PUBMED_17540563}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17540563 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17540563}}
 ==About this Structure==
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 [[Category: Carbonic anhydrase ii]]
 [[Category: Protein-inhibitor complex]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:25:43 2008''